Secondary literature sources for the SCAN domain

For each of the hand selected primary papers associated with the SCAN domain, 100 neighbouring papers are retrieved from PubMed. If one of these neighbouring papers is referenced by more than two primary papers, it is shown in the table below.

The zinc finger-associated SCAN box is a conserved oligomerization domain.

Williams AJ, Blacklow SC, Collins T
Mol Cell Biol. 1999; 19: 8526-35

A number of Cys(2)His(2) zinc finger proteins contain a highly conserved amino-terminal motif termed the SCAN domain. This element is an 80-residue, leucine-rich region that contains three segments strongly predicted to be alpha-helices. In this report, we show that the SCAN motif functions as an oligomerization domain mediating self-association or association with other proteins bearing SCAN domains. These findings suggest that the SCAN domain plays an important role in the assembly and function of this newly defined subclass of transcriptional regulators.